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Crystal structure of memo

Analyse Crystal structure of memo in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3BCZ
Type
protein
Length
1,171 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein MEMO1
UniProt
Q9Y316
Pockets
13 · best druggability 0.81

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, DProtein MEMO1protein29340% helix, 22% strandQ9Y316
CProtein MEMO1protein29240% helix, 23% strandQ9Y316

Ligands and binding sites

  • GOL · Glycerol · additive · 5 copies · chains A, B, C, D

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

13 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111360.810.8290empty
24060.570.7534empty
31470.500.7926empty
42230.490.7420empty
51240.440.7728empty

Interfaces

5 interfaces between chains.

  • A–B · 565 Ų buried · 7 hydrogen bonds · protein-protein
  • A–C · 459 Ų buried · 9 hydrogen bonds · protein-protein
  • B–D · 345 Ų buried · 2 hydrogen bonds · protein-protein
  • A–D · 300 Ų buried · 0 hydrogen bonds · protein-protein
  • B–C · 52 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 32 modified (engineered).

Compared structures

  • 3BCZ · Crystal structure of Memo · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9Y316 · AlphaFold monomer V2.0 prediction for protein MEMO1 (Q9Y316) · a predicted model of the same protein · chain C against A, TM-score 0.99

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